Regulation of membrane lipid synthesis in Escherichia coli after shifts in temperature

Okuyama, Harumi; Yamada, Kazuyo; Kameyama, Yasunaga; Ikezawa, Hiroh; Akamatsu, Yuzuru; Nojima, Shoshichi

doi:10.1021/bi00631a013

Cited by 67 publications

(24 citation statements)

References 34 publications

(36 reference statements)

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“…The decrease in phosphatidylinositol mannosides and simultaneous increase in phosphatidylethanolamine may have a protective role in maintaining membrane fluidity. Cardiolipin content has previously been found to be higher (Raziuddin, 1976 ;Dhariwal et al, 1977) or lower (De Siervo, 1969;Okuyama et al, 1977) in cells grown at 27 "C compared with those grown at 37 "C; no change in cardiolipin content was noted in this investigation with M . smegmatis.…”

Section: Results a N D Discussioncontrasting

confidence: 45%

“…The total lipid content of the bacteria was not significantly affected by the growth temperature but phospholipids were 45 % higher at 27 "C than at 37 "C. The lipid phosphorus content in both thermophilic and mesophilic bacteria has previously been observed to increase at higher temperatures (Ray et al, 1971 (Joyce et al, 1970) it has been found to increase at lower temperatures. It appears from our results, and the earlier work of De Siervo (1969), that at lower temperatures the synthesis of phospholipids is favoured, or alternatively the breakdown of phospholipids is slower.…”

Section: Results a N D Discussionmentioning

confidence: 76%

“…However, there was a 90 % increase in phosphatidylethanolamine at 27 "C (Table 1). Others (Raziuddin, 1976;Dhariwal et al, 1977;Okuyama et al, 1977;Khuller, 1977) have noted a decrease in phosphatidylethanolamine at lower temperature, although De Siervo (1 969) observed an increase in E. coli. The decrease in phosphatidylinositol mannosides and simultaneous increase in phosphatidylethanolamine may have a protective role in maintaining membrane fluidity.…”

Section: Results a N D Discussionmentioning

confidence: 96%

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Effect of Growth Temperature on the Lipid Composition of Mycobacterium smegmatis ATCC 607

Taneja

Malik

Khuller

1979

Journal of General Microbiology

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413The total lipid content of Mycobacterium smegmatis ATCC 607 was the same whether it was grown at 27 or 37 "C. The total phospholipid content, however, increased significantly at 27 "C. Phosphatidylethanolamine increased most markedly with a simultaneous decrease in phosphatidylinositol mannosides. Among individual phosphatidylinositol mannosides, tri-and tetra-acylated dimannophosphoinositides and tetra-acylated hexamannophosphoinositides all decreased at the lower growth temperature. Triacylglycerols and monoacylglycerols increased at the lower temperature but diacylglycerols were unaffected. Unsaturated fatty acids of total phospholipids increased as the temperature was lowered.

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Section: Results a N D Discussioncontrasting

confidence: 45%

Section: Results a N D Discussionmentioning

confidence: 76%

Section: Results a N D Discussionmentioning

confidence: 96%

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Effect of Growth Temperature on the Lipid Composition of Mycobacterium smegmatis ATCC 607

Taneja

Malik

Khuller

1979

Journal of General Microbiology

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“…In case of E. coli, membrane restructuring involves increase in the content of cisvaccenic (C18D 11 ) acid and decrease in palmitic acid (C16:0) (10). Cis-vaccenic acid is preferred over available palmitoleic (C16D 9 ) acid at lower temperature because cis-vaccenate (and not palmitoleate) can be incorporated at both the positions of glycerophospholipid, resulting in the formation of diunsaturated lipids which lowers the thermotropic transition of membranes (11,12,13). FabF catalyzes the elongation of C16D 9 to C18D 11 fatty acid.…”

Section: Introductionmentioning

confidence: 99%

β‐Ketoacyl‐ACP synthase I/II from Plasmodium falciparum (PfFabB/F)—Is it B or F?

Sharma

Surolia

et al. 2009

IUBMB Life

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Condensing enzymes play an important and decisive role in terms of fatty acid composition of any organism. They can be classified as condensing enzymes involved in initiating the cycle and enzymes involved in elongating the initiated fatty acyl chain. In E. coli, two isoforms for the elongation condensing enzymes (FabB and FabF) exists whereas Plasmodium genome contains only one isoform. By in vitro complementation studies in E. coli CY244 cells, we show that PfFabB/F functions like E. coli FabF as the growth of the mutant cells could be rescued only in the presence of oleic acid. But unlike bacterial enzyme, PfFabB/F does not increase the cis‐vaccenic acid content in the mutant cells upon lowering the growth temperature. This study thus highlights the distinct properties of P. falciparum FabF which sets it apart from E. coli and most other enzymes of this family described so far. © 2009 IUBMB IUBMB Life, 61(6): 658–662, 2009

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“…This regulation has been attributed to a temperature dependency of [3-ketoacyl-ACP synthase II in the last elongation reaction of the unsaturated pathway (8), but regulation at other points has also been suggested (19,20,28).…”

Section: Introductionmentioning

confidence: 99%

Role of escherichia coli β-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis

Siggaard-Andersen

1988

Carlsberg Res. Commun.

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Keywords: Cerulenin, fabB, fabF, 13-ketoacyl-ACP synthase II, fatty acid synthetase l'wo activities were found in E. coli extracts which could complement unsaturated fatty acid synthesis of a cerulenin treated E. coli fatty acid synthetase. One of these is []-ketoacyl-ACP synthase I, but it is not known whether the other activity represents the previously characterized 13-ketoacyl-ACP synthase 11. A mutant strain exhibiting a temperature sensitive unsaturated fatty acid synthetic activity apparently lacked an active 13-ketoacyl-ACP synthase 1.

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Regulation of membrane lipid synthesis in Escherichia coli after shifts in temperature

Cited by 67 publications

References 34 publications

Effect of Growth Temperature on the Lipid Composition of Mycobacterium smegmatis ATCC 607

Effect of Growth Temperature on the Lipid Composition of Mycobacterium smegmatis ATCC 607

β‐Ketoacyl‐ACP synthase I/II from Plasmodium falciparum (PfFabB/F)—Is it B or F?

Role of escherichia coli β-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis

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